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Biophys J, November 2002, p. 2705-2715, Vol. 83, No. 5
Department of Bioengineering, University of Washington, Seattle, Washington 98195 USA
In this report we characterized the longitudinal
elasticity of single actin filaments manipulated by novel
silicon-nitride microfabricated levers. Single actin filaments were
stretched from zero tension to maximal physiological tension,
P0. The obtained length-tension relation was
nonlinear in the low-tension range (0-50 pN) with a resultant strain
of ~0.4-0.6% and then became linear at moderate to high tensions
(~50-230 pN). In this region, the stretching stiffness of a single
rhodamine-phalloidin-labeled, 1-µm-long F-actin is 34.5 ± 3.5 pN/nm. Such a length-tension relation could be characterized by an
entropic-enthalpic worm-like chain model, which ascribes most of the
energy consumed in the nonlinear portion to overcoming thermal
undulations arising from the filament's interaction with surrounding
solution and the linear portion to the intrinsic stretching elasticity.
By fitting the experimental data with such a worm-like chain model, an
estimation of persistence length of ~8.75 µm was derived. These
results suggest that F-actin is more compliant than previously thought
and that thin filament compliance may account for a substantial
fraction of the sarcomere's elasticity.
Biophys J, November 2002, p. 2705-2715, Vol. 83, No. 5
© 2002 by the Biophysical Society 0006-3495/02/11/2705/11 $2.00
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